S-Nitrosylation of NSF controls membrane trafficking Journal Article
| Authors: | Söllner, T. H.; Sequeira, S. |
| Article Title: | S-Nitrosylation of NSF controls membrane trafficking |
| Abstract: | Nitric oxide is a diffusible molecule with profound effects on regulated exocytosis in several biological systems - however, the molecular targets remain elusive. In this issue of Cell, Matsushita et al. report that in aortic endothelial cells, S-nitrosylation of NSF, an ATPase essential for the activation of the membranefusion machinery, inhibits the exocytosis of Weibel-Palade bodies, secretory granules containing a cocktail of mediators essential to the regulation of vascular vessel tone. |
| Keywords: | protein phosphorylation; unclassified drug; nonhuman; protein analysis; cells, cultured; cell cycle; enzyme activity; endothelium cell; regulatory mechanism; amino acid sequence; conserved sequence; molecular sequence data; endothelium, vascular; enzyme inactivation; carrier proteins; cell membrane; short survey; inhibition kinetics; crystal structure; catalysis; structure analysis; adenosine triphosphatase; mutagenesis; reaction analysis; cysteine; protein modification; exocytosis; cell membrane transport; amino acid analysis; protein hydrolysis; nitric oxide; vesicular transport proteins; aorta; neurotransmission; membrane fusion; thrombocyte adhesion; secretory granule; humans; priority journal; n-ethylmaleimide-sensitive proteins; protein nsf; blood vessel tone; weibel palade body; weibel-palade bodies |
| Journal Title: | Cell |
| Volume: | 115 |
| Issue: | 2 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 2003-10-17 |
| Start Page: | 127 |
| End Page: | 129 |
| Language: | English |
| DOI: | 10.1016/s0092-8674(03)00811-0 |
| PUBMED: | 14567907 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 25 September 2014 -- Source: Scopus |
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